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Literature summary for 2.3.1.135 extracted from

  • Jahng, W.J.; Cheung, E.; Rando, R.R.
    Lecithin retinol acyltransferase forms functional homodimers (2002), Biochemistry, 41, 6311-6319.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00046
-
all-trans-retinol with dipalmitoylphosphatidylcholine, chemically dimerized enzyme Bos taurus
0.00052
-
all-trans-retinol with dipalmitoylphosphatidylcholine Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + all-trans-retinol Bos taurus
-
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
solubilization, centrifugation and dialysis Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + all-trans-retinol
-
Bos taurus all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
?

Subunits

Subunits Comment Organism
homodimer SDS-PAGE in absence of 2-mercaptoethanol Bos taurus
homodimer 2 × 25300, SDS-PAGE in presence of 2-mercaptoethanol Bos taurus
monomer
-
Bos taurus
More LRAT monomer interact in membranes and form functional homodimers, the dimer formation is mediated by disulfide bond formation and protein-protein interactions Bos taurus